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Database: UniProt
Entry: J2RCX1_9PSED
LinkDB: J2RCX1_9PSED
Original site: J2RCX1_9PSED 
ID   J2RCX1_9PSED            Unreviewed;       318 AA.
AC   J2RCX1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=tRNA U34 carboxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_01590};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01590};
GN   Name=cmoB {ECO:0000256|HAMAP-Rule:MF_01590};
GN   ORFNames=PMI26_01283 {ECO:0000313|EMBL:EJM46914.1};
OS   Pseudomonas sp. GM33.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1144329 {ECO:0000313|EMBL:EJM46914.1, ECO:0000313|Proteomes:UP000007274};
RN   [1] {ECO:0000313|EMBL:EJM46914.1, ECO:0000313|Proteomes:UP000007274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM33 {ECO:0000313|EMBL:EJM46914.1,
RC   ECO:0000313|Proteomes:UP000007274};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
CC   -!- FUNCTION: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-
CC       methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-
CC       carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_01590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine
CC         = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:52848, Rhea:RHEA-COMP:13381, Rhea:RHEA-
CC         COMP:13383, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:134278,
CC         ChEBI:CHEBI:136877, ChEBI:CHEBI:136879; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01590};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01590}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. CmoB family. {ECO:0000256|HAMAP-Rule:MF_01590}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01590}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJM46914.1}.
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DR   EMBL; AKJO01000036; EJM46914.1; -; Genomic_DNA.
DR   RefSeq; WP_007971754.1; NZ_AKJO01000036.1.
DR   AlphaFoldDB; J2RCX1; -.
DR   PATRIC; fig|1144329.3.peg.1266; -.
DR   Proteomes; UP000007274; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01590; tRNA_carboxymethyltr_CmoB; 1.
DR   InterPro; IPR010017; CmoB.
DR   InterPro; IPR027555; Mo5U34_MeTrfas-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00452; tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB; 1.
DR   PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43464:SF19; UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08003; Methyltransf_9; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:EJM46914.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01590, ECO:0000313|EMBL:EJM46914.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01590}.
FT   BINDING         88
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         102
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         107
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         126
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         192
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         196
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         311
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
SQ   SEQUENCE   318 AA;  36235 MW;  3A3D873322CAB3A0 CRC64;
     MIDLSPLARR LAGTPLAEWA NTLQAQLDKK MEKGHGDLER WQSALDALPK IQPSKVDLLN
     GLKLDTDCDD ETRAQMRSAL MGLSPWRKGP FDLFGVHVDT EWRSDWKWSR VAPHLDLVGK
     RILDVGCGNG YYMWRMLGAG ADSVIGVDPN WLFFCQFQAV QRYLSEPNAW HLPFPFEDLP
     PNLEGFDTVF SMGVFYHRRS PIEHLLALKD CLVKGGELVL ETLVVEGDKH QVLVPEDRYA
     QMRNVWFLPS VPALELWLRR AGFSDVRCVD VSTTTVEEQR GTEWMKYQSL SDFLDPEDHS
     KTIEGLPAPM RAVIVARK
//
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